Cross-talk between Arg methylation and Ser phosphorylation modulates apoptosis signal-regulating kinase 1 activation in endothelial cells

We describe a novel functional interaction between ASK1 and PRMT5. We show that PRMT5 interacts with and methylates ASK1 at arginine residue 89 and thereby negatively regulates its activity by promoting the interaction between ASK1 and Akt and thus phosphorylating ASK1 at serine residue 83. Furtherm...

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Veröffentlicht in:	Molecular biology of the cell 2016-04, Vol.27 (8), p.1358-1366
Hauptverfasser:	Chen, Ming, Qu, Xiaosheng, Zhang, Zhiqing, Wu, Huayu, Qin, Xia, Li, Fuji, Liu, Zhenfang, Tian, Liyuan, Miao, Jianhua, Shu, Wei
Format:	Artikel
Sprache:	eng
Schlagworte:	Arginine - metabolism Cell Line Endothelial Cells - drug effects Endothelial Cells - metabolism Enzyme Activation - drug effects Humans Hydrogen Peroxide - pharmacology MAP Kinase Kinase Kinase 5 - genetics MAP Kinase Kinase Kinase 5 - metabolism Methylation Phosphorylation Protein Interaction Mapping Protein-Arginine N-Methyltransferases - genetics Protein-Arginine N-Methyltransferases - metabolism Proto-Oncogene Proteins c-akt - metabolism Serine - metabolism Signal Transduction Vascular Endothelial Growth Factor A - pharmacology
Online-Zugang:	Volltext
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